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3btp
From Proteopedia
| 3btp | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||||
| Ligands: | , | ||||||||
| Gene: | virE2, Atu6190, AGR_pTi_28 (Agrobacterium tumefaciens str. C58), virE1, Atu6189, AGR_pTi_26 (Agrobacterium tumefaciens str. C58) | ||||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||
Contents |
Crystal structure of Agrobacterium tumefaciens VirE2 in complex with its chaperone VirE1: a novel fold and implications for DNA binding
Agrobacterium tumefaciens infects its plant hosts by a mechanism of horizontal gene transfer. This capability has led to its widespread use in artificial genetic transformation. In addition to DNA, the bacterium delivers an abundant ssDNA binding protein, VirE2, whose roles in the host include protection from cytoplasmic nucleases and adaptation for nuclear import. In Agrobacterium, VirE2 is bound to its acidic chaperone VirE1. When expressed in vitro in the absence of VirE1, VirE2 is prone to oligomerization and forms disordered filamentous aggregates. These filaments adopt an ordered solenoidal form in the presence of ssDNA, which was characterized previously by electron microscopy and three-dimensional image processing. VirE2 coexpressed in vitro with VirE1 forms a soluble heterodimer. VirE1 thus prevents VirE2 oligomerization and competes with its binding to ssDNA. We present here a crystal structure of VirE2 in complex with VirE1, showing that VirE2 is composed of two independent domains presenting a novel fold, joined by a flexible linker. Electrostatic interactions with VirE1 cement the two domains of VirE2 into a locked form. Comparison with the electron microscopy structure indicates that the VirE2 domains adopt different relative orientations. We suggest that the flexible linker between the domains enables VirE2 to accommodate its different binding partners.
Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners., Dym O, Albeck S, Unger T, Jacobovitch J, Branzburg A, Michael Y, Frenkiel-Krispin D, Wolf SG, Elbaum M, Proc Natl Acad Sci U S A. 2008 Aug 12;105(32):11170-5. Epub 2008 Aug 4. PMID:18678909
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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Additional Resources
For additional information, see: Nucleic Acids
Reference
Crystal structure of the Agrobacterium virulence complex VirE1-VirE2 reveals a flexible protein that can accommodate different partners., Dym O, Albeck S, Unger T, Jacobovitch J, Branzburg A, Michael Y, Frenkiel-Krispin D, Wolf G, Elbaum M., Proc Natl Acad Sci U S A. 2008 Aug 12. 105(32):11170-5 PMID:18678909
About this Structure
3BTP is a Protein complex structure of sequences from Agrobacterium tumefaciens str. c58. Full crystallographic information is available from OCA.
Page seeded by OCA on Wed Aug 20 11:45:29 2008
Proteopedia Page Contributors and Editors (what is this?)
Eran Hodis, OCA, David Canner, Alexander Berchansky, Jaime Prilusky
Categories: Albeck, S. | Branzburg, A. | Dym, O. | Jacobovitch, Y. | Michael, Y. | Unger, T. | ISPC, Israel Structural Proteomics Center. | Ispc | Israel structural proteomics center | Structural genomic | Agrobacterium tumefaciens str. c58 | Protein complex | Elbaum, M. | Chaperone | Crown gall tumor | Dna binding protein | Dna-binding | ISPC | Israel Structural Proteomics Center | Novel fold | Plasmid | Secreted | Tim barrel | Unique topology | Virulence | VirE2 fold
